DHE2_BACSU
ID DHE2_BACSU Reviewed; 424 AA.
AC P39633; Q53548; Q5W7E9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Catabolic NAD-specific glutamate dehydrogenase RocG;
DE Short=NAD-GDH;
DE EC=1.4.1.2 {ECO:0000269|PubMed:16244435, ECO:0000269|PubMed:20630473, ECO:0000269|PubMed:9829940};
DE AltName: Full=Glutamate dehydrogenase;
DE Short=GlutDH {ECO:0000303|PubMed:9829940};
DE AltName: Full=Trigger enzyme RocG;
GN Name=rocG {ECO:0000303|PubMed:9829940};
GN Synonyms=gudA {ECO:0000303|PubMed:9829940}, yweB;
GN OrderedLocusNames=BSU37790; ORFNames=ipa-75d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ISW1214;
RA Khan M.H., Itoh K., Kim H., Ashida H., Ishikawa T., Shibata H., Sawa Y.;
RT "Low thermostability of the NAD+ specific glutamate dehydrogenase from
RT Bacillus subtilis ISW1214: cloning, purification and characterization.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 324.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP PROTEIN SEQUENCE OF 1-15, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, MASS SPECTROMETRY, AND MUTAGENESIS OF GLU-27; GLN-144
RP AND ALA-324.
RC STRAIN=ISW1214;
RX PubMed=16244435; DOI=10.1271/bbb.69.1861;
RA Khan M.I., Ito K., Kim H., Ashida H., Ishikawa T., Shibata H., Sawa Y.;
RT "Molecular properties and enhancement of thermostability by random
RT mutagenesis of glutamate dehydrogenase from Bacillus subtilis.";
RL Biosci. Biotechnol. Biochem. 69:1861-1870(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 418-424.
RX PubMed=7565595; DOI=10.1007/bf02191600;
RA Klingel U., Miller C.M., North A.K., Stockley P.G., Baumberg S.;
RT "A binding site for activation by the Bacillus subtilis AhrC protein, a
RT repressor/activator of arginine metabolism.";
RL Mol. Gen. Genet. 248:329-340(1995).
RN [7]
RP FUNCTION AS A GLUTAMATE DEHYDROGENASE, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, SUBSTRATE SPECIFICITY, INDUCTION, AND NOMENCLATURE.
RC STRAIN=168 / SMY;
RX PubMed=9829940; DOI=10.1128/jb.180.23.6298-6305.1998;
RA Belitsky B.R., Sonenshein A.L.;
RT "Role and regulation of Bacillus subtilis glutamate dehydrogenase genes.";
RL J. Bacteriol. 180:6298-6305(1998).
RN [8]
RP INDUCTION.
RC STRAIN=168 / SMY;
RX PubMed=10468601; DOI=10.1073/pnas.96.18.10290;
RA Belitsky B.R., Sonenshein A.L.;
RT "An enhancer element located downstream of the major glutamate
RT dehydrogenase gene of Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10290-10295(1999).
RN [9]
RP FUNCTION IN THE CONTROL OF GLTAB EXPRESSION.
RX PubMed=17183217; DOI=10.1159/000096465;
RA Commichau F.M., Wacker I., Schleider J., Blencke H.M., Reif I., Tripal P.,
RA Stulke J.;
RT "Characterization of Bacillus subtilis mutants with carbon source-
RT independent glutamate biosynthesis.";
RL J. Mol. Microbiol. Biotechnol. 12:106-113(2007).
RN [10]
RP FUNCTION IN GLUTAMATE DEGRADATION.
RX PubMed=18326565; DOI=10.1128/jb.00099-08;
RA Commichau F.M., Gunka K., Landmann J.J., Stulke J.;
RT "Glutamate metabolism in Bacillus subtilis: gene expression and enzyme
RT activities evolved to avoid futile cycles and to allow rapid responses to
RT perturbations of the system.";
RL J. Bacteriol. 190:3557-3564(2008).
RN [11]
RP INDUCTION.
RX PubMed=15150224; DOI=10.1128/jb.186.11.3392-3398.2004;
RA Belitsky B.R., Kim H.J., Sonenshein A.L.;
RT "CcpA-dependent regulation of Bacillus subtilis glutamate dehydrogenase
RT gene expression.";
RL J. Bacteriol. 186:3392-3398(2004).
RN [12]
RP INHIBITORY INTERACTION WITH GLTC, AND SUBUNIT.
RX PubMed=17608797; DOI=10.1111/j.1365-2958.2007.05816.x;
RA Commichau F.M., Herzberg C., Tripal P., Valerius O., Stulke J.;
RT "A regulatory protein-protein interaction governs glutamate biosynthesis in
RT Bacillus subtilis: the glutamate dehydrogenase RocG moonlights in
RT controlling the transcription factor GltC.";
RL Mol. Microbiol. 65:642-654(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT LYS-93, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF GLU-93; ASP-122; TYR-158 AND SER-234, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=20630473; DOI=10.1016/j.jmb.2010.05.055;
RA Gunka K., Newman J.A., Commichau F.M., Herzberg C., Rodrigues C.,
RA Hewitt L., Lewis R.J., Stulke J.;
RT "Functional dissection of a trigger enzyme: mutations of the bacillus
RT subtilis glutamate dehydrogenase RocG that affect differentially its
RT catalytic activity and regulatory properties.";
RL J. Mol. Biol. 400:815-827(2010).
CC -!- FUNCTION: Devoted to catabolic function of glutamate (and other amino
CC acids of the glutamate family) utilization as sole nitrogen source. It
CC is not involved in anabolic function of glutamate biosynthesis since
CC B.subtilis possesses only one route of glutamate biosynthesis from
CC ammonia, catalyzed by glutamate synthase. Wild-type cells are unable to
CC utilize glutamate or glutamine as a sole carbon source; thus RocG does
CC not function physiologically to synthesize glutamate, but it is
CC involved in the utilization of arginine, and proline as carbon or
CC nitrogen source (PubMed:9829940). The catabolic RocG is essential for
CC controlling gltAB expression via an inhibitory interactions with the
CC transcriptional regulator GltC in response to the availability of
CC sugars (PubMed:17183217, PubMed:15150224).
CC {ECO:0000269|PubMed:15150224, ECO:0000269|PubMed:17183217,
CC ECO:0000269|PubMed:9829940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2;
CC Evidence={ECO:0000269|PubMed:16244435, ECO:0000269|PubMed:9829940};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15134;
CC Evidence={ECO:0000269|PubMed:16244435, ECO:0000269|PubMed:20630473};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.08 mM for NAD (at 37 degrees Celsius and at pH 7.3)
CC {ECO:0000269|PubMed:16244435, ECO:0000269|PubMed:20630473};
CC KM=0.34 mM for L-glutamate (at 37 degrees Celsius and at pH 7.3)
CC {ECO:0000269|PubMed:16244435, ECO:0000269|PubMed:20630473};
CC KM=2.9 mM for L-glutamate (at 37 degrees Celsius and at pH 7.3)
CC {ECO:0000269|PubMed:16244435, ECO:0000269|PubMed:20630473};
CC KM=0.65 mM for 2-oxoglutarate (at 37 degrees Celsius and at pH 7.3)
CC {ECO:0000269|PubMed:16244435, ECO:0000269|PubMed:20630473};
CC KM=2.9 mM for L-glutamate (at pH 7.3) {ECO:0000269|PubMed:16244435,
CC ECO:0000269|PubMed:20630473};
CC KM=18.5 mM for ammonium (at pH 7.7) {ECO:0000269|PubMed:16244435,
CC ECO:0000269|PubMed:20630473};
CC KM=55.6 mM for ammonium (at 37 degrees Celsius and at pH 7.3)
CC {ECO:0000269|PubMed:16244435, ECO:0000269|PubMed:20630473};
CC pH dependence:
CC Optimum pH is 7.7 and 7.3 for L-glutamate deamination and 2-
CC oxoglutarate amination, respectively. Half-maximal activity for
CC deamination is observed at pH 6.9 and 7.8 and that for amination is
CC at pH 6.9 and 7.8. {ECO:0000269|PubMed:16244435,
CC ECO:0000269|PubMed:20630473};
CC Temperature dependence:
CC Low thermostability at 41 degrees Celsius due to the dissociation of
CC the hexamer. {ECO:0000269|PubMed:16244435,
CC ECO:0000269|PubMed:20630473};
CC -!- SUBUNIT: Homohexamer (PubMed:16244435, PubMed:20630473). Interacts with
CC transcriptional regulator GltC (PubMed:17608797).
CC {ECO:0000269|PubMed:16244435, ECO:0000269|PubMed:17608797,
CC ECO:0000269|PubMed:20630473}.
CC -!- INTERACTION:
CC P39633; P20668: gltC; NbExp=2; IntAct=EBI-1642022, EBI-1642006;
CC -!- INDUCTION: Enzyme activity is low in early exponential phase and
CC reached higher levels in the middle and late stages of exponential
CC growth (at protein level). Repressed by glucose; induced by arginine,
CC ornithine, or to a lesser extent proline (in the absence of glucose).
CC Not induced by glutamate or glutamine (PubMed:9829940). Expression
CC depends on the alternative sigma-L factor and the transcription factor
CC RocR (PubMed:10468601). Subject to direct CcpA-dependent glucose
CC repression (PubMed:15150224). {ECO:0000269|PubMed:10468601,
CC ECO:0000269|PubMed:15150224, ECO:0000269|PubMed:9829940}.
CC -!- MASS SPECTROMETRY: Mass=46587; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16244435};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to
CC utilize proline, ornithine, or arginine as sole carbon source and grow
CC more slowly when proline or ornithine is utilized as sole nitrogen
CC source in the presence of glucose. A double rocG-gudB disruption has
CC the same phenotype as a single rocG disruption.
CC {ECO:0000269|PubMed:9829940}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; X73124; CAA51631.1; -; Genomic_DNA.
DR EMBL; AB194695; BAD69594.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15806.2; -; Genomic_DNA.
DR EMBL; S79622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A70055; A70055.
DR RefSeq; NP_391659.2; NC_000964.3.
DR RefSeq; WP_003227482.1; NZ_JNCM01000034.1.
DR PDB; 3K92; X-ray; 2.30 A; A/B/C/D/E/F=1-424.
DR PDBsum; 3K92; -.
DR AlphaFoldDB; P39633; -.
DR SMR; P39633; -.
DR IntAct; P39633; 1.
DR STRING; 224308.BSU37790; -.
DR MoonProt; P39633; -.
DR jPOST; P39633; -.
DR PaxDb; P39633; -.
DR PRIDE; P39633; -.
DR EnsemblBacteria; CAB15806; CAB15806; BSU_37790.
DR GeneID; 937066; -.
DR KEGG; bsu:BSU37790; -.
DR PATRIC; fig|224308.179.peg.4091; -.
DR eggNOG; COG0334; Bacteria.
DR InParanoid; P39633; -.
DR OMA; TNAWWWW; -.
DR PhylomeDB; P39633; -.
DR BioCyc; BSUB:BSU37790-MON; -.
DR BRENDA; 1.4.1.2; 658.
DR SABIO-RK; P39633; -.
DR EvolutionaryTrace; P39633; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IMP:UniProtKB.
DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000185; Glu_DH; 1.
DR PRINTS; PR00082; GLFDHDRGNASE.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..424
FT /note="Catabolic NAD-specific glutamate dehydrogenase RocG"
FT /id="PRO_0000182735"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 156
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT MUTAGEN 27
FT /note="E->F: Increase of thermostability 8 degrees Celsius
FT higher than that of the wild-type."
FT /evidence="ECO:0000269|PubMed:16244435"
FT MUTAGEN 93
FT /note="E->K: Reduces the affinity for glutamate and
FT ammonium."
FT /evidence="ECO:0000269|PubMed:20630473"
FT MUTAGEN 122
FT /note="D->N: Unable to control gltAB expression via an
FT inhibitory interactions with the transcriptional regulator
FT GltC. Reduces the affinity for glutamate and ammonium."
FT /evidence="ECO:0000269|PubMed:20630473"
FT MUTAGEN 144
FT /note="Q->R: Increase of thermostability 20 degrees Celsius
FT higher than that of the wild-type."
FT /evidence="ECO:0000269|PubMed:16244435"
FT MUTAGEN 158
FT /note="Y->H: Reduces the affinity for glutamate and
FT ammonium."
FT /evidence="ECO:0000269|PubMed:20630473"
FT MUTAGEN 234
FT /note="S->R: Reduces the affinity for glutamate and
FT ammonium."
FT /evidence="ECO:0000269|PubMed:20630473"
FT MUTAGEN 324
FT /note="A->R: No effect."
FT /evidence="ECO:0000269|PubMed:16244435"
FT CONFLICT 324
FT /note="A -> R (in Ref. 1; CAA51631)"
FT /evidence="ECO:0000305"
FT CONFLICT 419..424
FT /note="RFRGWV -> FPRMGLI (in Ref. 1; CAA51631)"
FT /evidence="ECO:0000305"
FT HELIX 8..31
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 91..107
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 128..142
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3K92"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3K92"
FT TURN 194..198
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:3K92"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:3K92"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 353..367
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 373..398
FT /evidence="ECO:0007829|PDB:3K92"
FT HELIX 402..420
FT /evidence="ECO:0007829|PDB:3K92"
SQ SEQUENCE 424 AA; 46553 MW; 019AE0A833BE48DD CRC64;
MSAKQVSKDE EKEALNLFLS TQTIIKEALR KLGYPGDMYE LMKEPQRMLT VRIPVKMDNG
SVKVFTGYRS QHNDAVGPTK GGVRFHPEVN EEEVKALSIW MTLKCGIANL PYGGGKGGII
CDPRTMSFGE LERLSRGYVR AISQIVGPTK DIPAPDVYTN SQIMAWMMDE YSRLREFDSP
GFITGKPLVL GGSQGRETAT AQGVTICIEE AVKKKGIKLQ NARIIIQGFG NAGSFLAKFM
HDAGAKVIGI SDANGGLYNP DGLDIPYLLD KRDSFGMVTN LFTDVITNEE LLEKDCDILV
PAAISNQITA KNAHNIQASI VVEAANGPTT IDATKILNER GVLLVPDILA SAGGVTVSYF
EWVQNNQGYY WSEEEVAEKL RSVMVSSFET IYQTAATHKV DMRLAAYMTG IRKSAEASRF
RGWV
